Intrinsically disordered CsoS2 acts as a general molecular thread for α-carboxysome shell assembly

Tao Ni (), Qiuyao Jiang, Pei Cing Ng, Juan Shen, Hao Dou, Yanan Zhu, Julika Radecke, Gregory F. Dykes, Fang Huang, Lu-Ning Liu () and Peijun Zhang ()
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Tao Ni: University of Oxford
Qiuyao Jiang: University of Liverpool
Pei Cing Ng: University of Liverpool
Juan Shen: University of Oxford
Hao Dou: University of Oxford
Yanan Zhu: University of Oxford
Julika Radecke: Diamond Light Source, Harwell Science and Innovation Campus
Gregory F. Dykes: University of Liverpool
Fang Huang: University of Liverpool
Lu-Ning Liu: University of Liverpool
Peijun Zhang: University of Oxford

Nature Communications, 2023, vol. 14, issue 1, 1-9

Abstract: Abstract Carboxysomes are a paradigm of self-assembling proteinaceous organelles found in nature, offering compartmentalisation of enzymes and pathways to enhance carbon fixation. In α-carboxysomes, the disordered linker protein CsoS2 plays an essential role in carboxysome assembly and Rubisco encapsulation. Its mechanism of action, however, is not fully understood. Here we synthetically engineer α-carboxysome shells using minimal shell components and determine cryoEM structures of these to decipher the principle of shell assembly and encapsulation. The structures reveal that the intrinsically disordered CsoS2 C-terminus is well-structured and acts as a universal “molecular thread” stitching through multiple shell protein interfaces. We further uncover in CsoS2 a highly conserved repetitive key interaction motif, [IV]TG, which is critical to the shell assembly and architecture. Our study provides a general mechanism for the CsoS2-governed carboxysome shell assembly and cargo encapsulation and further advances synthetic engineering of carboxysomes for diverse biotechnological applications.

Date: 2023
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DOI: 10.1038/s41467-023-41211-y

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